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Database: PDB
Entry: 3LSF
LinkDB: 3LSF
Original site: 3LSF 
HEADER    TRANSPORT PROTEIN                       12-FEB-10   3LSF              
TITLE     PIRACETAM BOUND TO THE LIGAND BINDING DOMAIN OF GLUA2                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: B, E, H;                                                      
COMPND   4 SYNONYM: GLUR-2, GLUR-B, GLUR-K2, GLUTAMATE RECEPTOR IONOTROPIC, AMPA
COMPND   5 2, AMPA-SELECTIVE GLUTAMATE RECEPTOR 2;                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: GRIA2, GLUR2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-22B(+)                                
KEYWDS    GLUTAMATE RECEPTOR, GLUR2, GLUA2, AMPA RECEPTOR, NEUROTRANSMITTER     
KEYWDS   2 RECEPTOR, S1S2, ALLOSTERIC MODULATOR, ALTERNATIVE SPLICING, CELL     
KEYWDS   3 JUNCTION, CELL MEMBRANE, ENDOPLASMIC RETICULUM, GLYCOPROTEIN, ION    
KEYWDS   4 TRANSPORT, IONIC CHANNEL, MEMBRANE, PHOSPHOPROTEIN, POSTSYNAPTIC     
KEYWDS   5 CELL MEMBRANE, RECEPTOR, RNA EDITING, SYNAPSE, TRANSMEMBRANE,        
KEYWDS   6 TRANSPORT, TRANSPORT PROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.H.AHMED,C.P.PTAK,R.E.OSWALD                                         
REVDAT   2   02-AUG-17 3LSF    1       SOURCE                                   
REVDAT   1   16-MAR-10 3LSF    0                                                
JRNL        AUTH   A.H.AHMED,R.E.OSWALD                                         
JRNL        TITL   PIRACETAM DEFINES A NEW BINDING SITE FOR ALLOSTERIC          
JRNL        TITL 2 MODULATORS OF                                                
JRNL        TITL 3 ALPHA-AMINO-3-HYDROXY-5-METHYL-4-ISOXAZOLE-PROPIONIC ACID    
JRNL        TITL 4 (AMPA) RECEPTORS.                                            
JRNL        REF    J.MED.CHEM.                   V.  53  2197 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20163115                                                     
JRNL        DOI    10.1021/JM901905J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.110                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 71963                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.670                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1918                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.2607 -  4.4575    0.99     5616   152  0.2143 0.2101        
REMARK   3     2  4.4575 -  3.5393    0.99     5404   146  0.1726 0.2161        
REMARK   3     3  3.5393 -  3.0923    0.99     5300   145  0.1809 0.1857        
REMARK   3     4  3.0923 -  2.8097    0.99     5293   147  0.1977 0.2121        
REMARK   3     5  2.8097 -  2.6084    0.98     5247   141  0.2014 0.2497        
REMARK   3     6  2.6084 -  2.4547    0.98     5173   143  0.2002 0.2219        
REMARK   3     7  2.4547 -  2.3318    0.97     5112   140  0.1986 0.2588        
REMARK   3     8  2.3318 -  2.2303    0.96     5100   140  0.1887 0.2521        
REMARK   3     9  2.2303 -  2.1445    0.96     5053   140  0.1814 0.2150        
REMARK   3    10  2.1445 -  2.0705    0.95     5032   138  0.1823 0.2188        
REMARK   3    11  2.0705 -  2.0057    0.94     4921   136  0.1868 0.2651        
REMARK   3    12  2.0057 -  1.9484    0.89     4651   133  0.2099 0.2452        
REMARK   3    13  1.9484 -  1.8971    0.84     4368   118  0.2167 0.2980        
REMARK   3    14  1.8971 -  1.8510    0.71     3775    99  0.2317 0.2702        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.39                                          
REMARK   3   B_SOL              : 49.84                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.780           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 3.49                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.62960                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : -6.05100                                             
REMARK   3    B13 (A**2) : -4.80380                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           6268                                  
REMARK   3   ANGLE     :  1.073           8417                                  
REMARK   3   CHIRALITY :  0.070            921                                  
REMARK   3   PLANARITY :  0.007           1054                                  
REMARK   3   DIHEDRAL  : 15.382           2307                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3LSF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057671.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977                              
REMARK 200  MONOCHROMATOR                  : RH COATED SI                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71963                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5930                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.53200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.186                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3DP6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-18% PEG8K, 0.1 M NA CACODYLATE, 0.1   
REMARK 280  -0.15 M ZINC ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.01150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.88950            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.01150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       81.88950            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      114.02300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      163.77900            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN H 235    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU H   166    ZN     ZN H     2              1.64            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS B 218     -164.46   -160.18                                   
REMARK 500    ASN E  22       43.48   -108.12                                   
REMARK 500    LYS H  21      -84.68    -20.15                                   
REMARK 500    LEU H  26     -175.64    -69.98                                   
REMARK 500    TRP H 255      -63.73   -100.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  46   NE2                                                    
REMARK 620 2 GLU H  42   OE2  95.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  42   OE2                                                    
REMARK 620 2 HIS E  46   NE2  86.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   NE2                                                    
REMARK 620 2 GLU B  42   OE2  87.1                                              
REMARK 620 3 GLU H 166   OE2  93.7 154.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PZI B 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU E 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PZI B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU H 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PZI E 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PZI E 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PZI H 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PZI H 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LSL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3LSW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3LSX   RELATED DB: PDB                                   
DBREF  3LSF B    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3LSF B  120   261  UNP    P19491   GRIA2_RAT      653    794             
DBREF  3LSF E    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3LSF E  120   261  UNP    P19491   GRIA2_RAT      653    794             
DBREF  3LSF H    4   117  UNP    P19491   GRIA2_RAT      414    527             
DBREF  3LSF H  120   261  UNP    P19491   GRIA2_RAT      653    794             
SEQADV 3LSF GLY B  118  UNP  P19491              LINKER                         
SEQADV 3LSF THR B  119  UNP  P19491              LINKER                         
SEQADV 3LSF SER B  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQADV 3LSF GLY E  118  UNP  P19491              LINKER                         
SEQADV 3LSF THR E  119  UNP  P19491              LINKER                         
SEQADV 3LSF SER E  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQADV 3LSF GLY H  118  UNP  P19491              LINKER                         
SEQADV 3LSF THR H  119  UNP  P19491              LINKER                         
SEQADV 3LSF SER H  242  UNP  P19491    ASN   775 ENGINEERED                     
SEQRES   1 B  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 B  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 B  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 B  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 B  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 B  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 B  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 B  258  VAL ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 B  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 B  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 B  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU PHE          
SEQRES  12 B  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 B  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 B  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 B  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 B  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 B  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 B  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 B  258  VAL LEU LYS LEU SER GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 B  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
SEQRES   1 E  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 E  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 E  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 E  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 E  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 E  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 E  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 E  258  VAL ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 E  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 E  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 E  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU PHE          
SEQRES  12 E  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 E  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 E  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 E  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 E  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 E  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 E  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 E  258  VAL LEU LYS LEU SER GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 E  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
SEQRES   1 H  258  LYS THR VAL VAL VAL THR THR ILE LEU GLU SER PRO TYR          
SEQRES   2 H  258  VAL MET MET LYS LYS ASN HIS GLU MET LEU GLU GLY ASN          
SEQRES   3 H  258  GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU ALA ALA GLU          
SEQRES   4 H  258  ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS LEU THR ILE          
SEQRES   5 H  258  VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP ALA ASP THR          
SEQRES   6 H  258  LYS ILE TRP ASN GLY MET VAL GLY GLU LEU VAL TYR GLY          
SEQRES   7 H  258  LYS ALA ASP ILE ALA ILE ALA PRO LEU THR ILE THR LEU          
SEQRES   8 H  258  VAL ARG GLU GLU VAL ILE ASP PHE SER LYS PRO PHE MET          
SEQRES   9 H  258  SER LEU GLY ILE SER ILE MET ILE LYS LYS GLY THR PRO          
SEQRES  10 H  258  ILE GLU SER ALA GLU ASP LEU SER LYS GLN THR GLU ILE          
SEQRES  11 H  258  ALA TYR GLY THR LEU ASP SER GLY SER THR LYS GLU PHE          
SEQRES  12 H  258  PHE ARG ARG SER LYS ILE ALA VAL PHE ASP LYS MET TRP          
SEQRES  13 H  258  THR TYR MET ARG SER ALA GLU PRO SER VAL PHE VAL ARG          
SEQRES  14 H  258  THR THR ALA GLU GLY VAL ALA ARG VAL ARG LYS SER LYS          
SEQRES  15 H  258  GLY LYS TYR ALA TYR LEU LEU GLU SER THR MET ASN GLU          
SEQRES  16 H  258  TYR ILE GLU GLN ARG LYS PRO CYS ASP THR MET LYS VAL          
SEQRES  17 H  258  GLY GLY ASN LEU ASP SER LYS GLY TYR GLY ILE ALA THR          
SEQRES  18 H  258  PRO LYS GLY SER SER LEU GLY ASN ALA VAL ASN LEU ALA          
SEQRES  19 H  258  VAL LEU LYS LEU SER GLU GLN GLY LEU LEU ASP LYS LEU          
SEQRES  20 H  258  LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU CYS                  
HET    GLU  B 400      10                                                       
HET    PZI  B 800      20                                                       
HET    PZI  B 802      10                                                       
HET    GLU  E 400      10                                                       
HET    PZI  E 802      10                                                       
HET    PZI  E 800      20                                                       
HET     ZN  E   1       1                                                       
HET     ZN  E   3       1                                                       
HET     ZN  E 401       1                                                       
HET    GLU  H 400      10                                                       
HET    PZI  H 800      20                                                       
HET    PZI  H 802      10                                                       
HET     ZN  H   2       1                                                       
HET     ZN  H 401       1                                                       
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     PZI 2-(2-OXOPYRROLIDIN-1-YL)ACETAMIDE                                
HETNAM      ZN ZINC ION                                                         
FORMUL   4  GLU    3(C5 H9 N O4)                                                
FORMUL   5  PZI    6(C6 H10 N2 O2)                                              
FORMUL  10   ZN    5(ZN 2+)                                                     
FORMUL  18  HOH   *867(H2 O)                                                    
HELIX    1   1 ASN B   22  LEU B   26  5                                   5    
HELIX    2   2 GLU B   27  GLU B   30  5                                   4    
HELIX    3   3 GLY B   34  GLY B   48  1                                  15    
HELIX    4   4 ASN B   72  TYR B   80  1                                   9    
HELIX    5   5 THR B   93  GLU B   98  1                                   6    
HELIX    6   6 SER B  123  LYS B  129  1                                   7    
HELIX    7   7 GLY B  141  SER B  150  1                                  10    
HELIX    8   8 ILE B  152  ALA B  165  1                                  14    
HELIX    9   9 THR B  173  SER B  184  1                                  12    
HELIX   10  10 SER B  194  GLN B  202  1                                   9    
HELIX   11  11 SER B  229  GLN B  244  1                                  16    
HELIX   12  12 GLY B  245  TYR B  256  1                                  12    
HELIX   13  13 ASN E   22  LEU E   26  5                                   5    
HELIX   14  14 GLU E   27  GLU E   30  5                                   4    
HELIX   15  15 GLY E   34  GLY E   48  1                                  15    
HELIX   16  16 ASN E   72  TYR E   80  1                                   9    
HELIX   17  17 THR E   93  GLU E   98  1                                   6    
HELIX   18  18 SER E  123  LYS E  129  1                                   7    
HELIX   19  19 GLY E  141  SER E  150  1                                  10    
HELIX   20  20 ILE E  152  ALA E  165  1                                  14    
HELIX   21  21 THR E  173  SER E  184  1                                  12    
HELIX   22  22 SER E  194  GLN E  202  1                                   9    
HELIX   23  23 LEU E  230  GLN E  244  1                                  15    
HELIX   24  24 GLY E  245  TRP E  255  1                                  11    
HELIX   25  25 GLY H   28  GLU H   30  5                                   3    
HELIX   26  26 GLY H   34  GLY H   48  1                                  15    
HELIX   27  27 ASN H   72  TYR H   80  1                                   9    
HELIX   28  28 THR H   93  GLU H   98  1                                   6    
HELIX   29  29 SER H  123  LYS H  129  1                                   7    
HELIX   30  30 GLY H  141  SER H  150  1                                  10    
HELIX   31  31 ILE H  152  ALA H  165  1                                  14    
HELIX   32  32 THR H  173  SER H  184  1                                  12    
HELIX   33  33 SER H  194  GLN H  202  1                                   9    
HELIX   34  34 SER H  229  GLN H  244  1                                  16    
HELIX   35  35 GLY H  245  TRP H  255  1                                  11    
SHEET    1   A 3 TYR B  51  ILE B  55  0                                        
SHEET    2   A 3 VAL B   6  THR B  10  1  N  VAL B   8   O  LYS B  52           
SHEET    3   A 3 ILE B  85  ALA B  86  1  O  ILE B  85   N  THR B   9           
SHEET    1   B 2 MET B  18  MET B  19  0                                        
SHEET    2   B 2 TYR B  32  GLU B  33 -1  O  GLU B  33   N  MET B  18           
SHEET    1   C 2 ILE B 100  PHE B 102  0                                        
SHEET    2   C 2 ALA B 223  PRO B 225 -1  O  THR B 224   N  ASP B 101           
SHEET    1   D 2 MET B 107  LEU B 109  0                                        
SHEET    2   D 2 LYS B 218  TYR B 220 -1  O  LYS B 218   N  LEU B 109           
SHEET    1   E 4 ALA B 134  THR B 137  0                                        
SHEET    2   E 4 TYR B 188  GLU B 193  1  O  LEU B 191   N  GLY B 136           
SHEET    3   E 4 ILE B 111  LYS B 116 -1  N  MET B 114   O  TYR B 190           
SHEET    4   E 4 THR B 208  VAL B 211 -1  O  MET B 209   N  ILE B 115           
SHEET    1   F 3 LYS E  50  ILE E  55  0                                        
SHEET    2   F 3 THR E   5  THR E  10  1  N  VAL E   6   O  LYS E  50           
SHEET    3   F 3 ILE E  85  ALA E  86  1  O  ILE E  85   N  THR E   9           
SHEET    1   G 2 MET E  18  MET E  19  0                                        
SHEET    2   G 2 TYR E  32  GLU E  33 -1  O  GLU E  33   N  MET E  18           
SHEET    1   H 2 ILE E 100  PHE E 102  0                                        
SHEET    2   H 2 ALA E 223  PRO E 225 -1  O  THR E 224   N  ASP E 101           
SHEET    1   I 2 MET E 107  LEU E 109  0                                        
SHEET    2   I 2 LYS E 218  TYR E 220 -1  O  LYS E 218   N  LEU E 109           
SHEET    1   J 4 ALA E 134  GLY E 136  0                                        
SHEET    2   J 4 TYR E 188  GLU E 193  1  O  LEU E 191   N  GLY E 136           
SHEET    3   J 4 ILE E 111  LYS E 116 -1  N  SER E 112   O  LEU E 192           
SHEET    4   J 4 THR E 208  VAL E 211 -1  O  MET E 209   N  ILE E 115           
SHEET    1   K 3 TYR H  51  ILE H  55  0                                        
SHEET    2   K 3 VAL H   6  THR H  10  1  N  VAL H   8   O  LYS H  52           
SHEET    3   K 3 ILE H  85  ALA H  86  1  O  ILE H  85   N  THR H   9           
SHEET    1   L 2 MET H  18  MET H  19  0                                        
SHEET    2   L 2 TYR H  32  GLU H  33 -1  O  GLU H  33   N  MET H  18           
SHEET    1   M 2 ILE H 100  PHE H 102  0                                        
SHEET    2   M 2 ALA H 223  PRO H 225 -1  O  THR H 224   N  ASP H 101           
SHEET    1   N 2 MET H 107  LEU H 109  0                                        
SHEET    2   N 2 LYS H 218  TYR H 220 -1  O  LYS H 218   N  LEU H 109           
SHEET    1   O 4 ALA H 134  THR H 137  0                                        
SHEET    2   O 4 TYR H 188  GLU H 193  1  O  LEU H 191   N  GLY H 136           
SHEET    3   O 4 ILE H 111  LYS H 116 -1  N  SER H 112   O  LEU H 192           
SHEET    4   O 4 THR H 208  VAL H 211 -1  O  MET H 209   N  ILE H 115           
SSBOND   1 CYS B  206    CYS B  261                          1555   1555  2.03  
SSBOND   2 CYS E  206    CYS E  261                          1555   1555  2.04  
SSBOND   3 CYS H  206    CYS H  261                          1555   1555  2.04  
LINK         NE2 HIS H  46                ZN    ZN H 401     1555   1555  1.91  
LINK         OE2 GLU E  42                ZN    ZN E 401     1555   1555  1.99  
LINK         NE2 HIS B  46                ZN    ZN H   2     1555   1555  2.09  
LINK         OD2 ASP E  65                ZN    ZN E   1     1555   1555  2.11  
LINK         NE2 HIS E  23                ZN    ZN E   3     1555   1555  2.13  
LINK         NE2 HIS E  46                ZN    ZN E 401     1555   1555  2.32  
LINK         OE2 GLU B  42                ZN    ZN H   2     1555   1555  2.34  
LINK         OE2 GLU H 166                ZN    ZN H   2     1555   1555  2.40  
LINK         OE2 GLU H  42                ZN    ZN H 401     1555   1555  2.41  
CISPEP   1 SER B   14    PRO B   15          0        -2.05                     
CISPEP   2 GLU B  166    PRO B  167          0        -1.78                     
CISPEP   3 LYS B  204    PRO B  205          0         7.29                     
CISPEP   4 SER E   14    PRO E   15          0        -2.51                     
CISPEP   5 GLU E  166    PRO E  167          0        -3.42                     
CISPEP   6 LYS E  204    PRO E  205          0         9.89                     
CISPEP   7 SER H   14    PRO H   15          0        -3.91                     
CISPEP   8 GLU H  166    PRO H  167          0        -2.49                     
CISPEP   9 LYS H  204    PRO H  205          0         7.11                     
SITE     1 AC1 13 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 AC1 13 ARG B  96  GLY B 141  SER B 142  THR B 143                    
SITE     3 AC1 13 GLU B 193  TYR B 220  HOH B 401  HOH B 411                    
SITE     4 AC1 13 HOH B 470                                                     
SITE     1 AC2 18 TYR B  35  PRO B 105  PHE B 106  MET B 107                    
SITE     2 AC2 18 SER B 108  SER B 242  LEU B 247  ASP B 248                    
SITE     3 AC2 18 HOH B 405  HOH B 454  HOH B 460  HOH B 553                    
SITE     4 AC2 18 HOH B 652  PRO E 105  SER E 217  LYS E 218                    
SITE     5 AC2 18 GLY E 219  PZI E 800                                          
SITE     1 AC3 14 TYR E  61  PRO E  89  LEU E  90  THR E  91                    
SITE     2 AC3 14 ARG E  96  LEU E 138  GLY E 141  SER E 142                    
SITE     3 AC3 14 THR E 143  GLU E 193  TYR E 220  HOH E 289                    
SITE     4 AC3 14 HOH E 292  HOH E 352                                          
SITE     1 AC4  5 ASP B 216  SER B 217  HOH B 449  ASP E 248                    
SITE     2 AC4  5 ASN E 252                                                     
SITE     1 AC5 12 TYR H  61  PRO H  89  LEU H  90  THR H  91                    
SITE     2 AC5 12 ARG H  96  GLY H 141  SER H 142  THR H 143                    
SITE     3 AC5 12 GLU H 193  HOH H 528  HOH H 540  HOH H 549                    
SITE     1 AC6  6 ASP B 248  ASN B 252  ASP E 216  SER E 217                    
SITE     2 AC6  6 HOH E 509  HOH E 858                                          
SITE     1 AC7 18 PRO B 105  SER B 108  SER B 217  LYS B 218                    
SITE     2 AC7 18 GLY B 219  PZI B 800  PRO E 105  PHE E 106                    
SITE     3 AC7 18 MET E 107  SER E 108  SER E 242  LEU E 247                    
SITE     4 AC7 18 ASP E 248  LYS E 251  HOH E 307  HOH E 375                    
SITE     5 AC7 18 HOH E 493  HOH E 507                                          
SITE     1 AC8 15 PRO H 105  PHE H 106  MET H 107  SER H 108                    
SITE     2 AC8 15 SER H 217  LYS H 218  GLY H 219  SER H 242                    
SITE     3 AC8 15 LEU H 247  ASP H 248  HOH H 539  HOH H 559                    
SITE     4 AC8 15 HOH H 583  HOH H 639  HOH H 687                               
SITE     1 AC9  6 ASN H 214  ASP H 216  SER H 217  ASP H 248                    
SITE     2 AC9  6 HOH H 815  HOH H 828                                          
SITE     1 BC1  2 HIS B  23  ASP E  65                                          
SITE     1 BC2  4 HIS E  23  GLU E  24  HIS H  23  GLU H  30                    
SITE     1 BC3  3 GLU E  42  HIS E  46  GLN E 244                               
SITE     1 BC4  3 GLU B  42  HIS B  46  GLU H 166                               
SITE     1 BC5  5 GLU B 166  GLU H  42  HIS H  46  LEU H 241                    
SITE     2 BC5  5 GLN H 244                                                     
CRYST1   47.275  114.023  163.779  90.00  90.00  90.00 P 2 21 21    12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021153  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006106        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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